Allelic variation in a simple sequence repeat element of neisserial pglB2 and its consequences for protein expression and protein glycosylation

6Citations
Citations of this article
13Readers
Mendeley users who have this article in their library.

This article is free to access.

Abstract

Neisseria species express an O-linked glycosylation system in which functionally distinct proteins are elaborated with variable glycans. A major source of glycan diversity in N. meningitidis results from two distinct pglB alleles responsible for the synthesis of either N,N'-diacetylbacillosamine or glyceramido-acetamido trideoxyhexose that occupy the reducing end of the oligosaccharides. Alternative modifications at C-4 of the precursor UDP-4-amino are attributable to distinct C-terminal domains that dictate either acetyltransferase or glyceramidotransferase activity, encoded by pglB and pglB2, respectively. Naturally occurring alleles of pglB2 have homopolymeric tracts of either 7 or 8 adenosines (As) bridging the C-terminal open reading frame (ORF) and the ORF encompassing the conserved N-terminal domain associated with phosphoglycosyltransferase activity. In the work presented here, we explored the consequences of such pglB2 allele variation and found that, although both alleles are functional vis-à-vis glycosylation, the 7A form results in the expression of a single, multidomain protein, while the 8A variant elicits two single-domain proteins. We also found that the glyceramidotransferase activity-encoding domain is essential to protein glycosylaton, showing the critical role of the C-4 modification of the precursor UDP-4-amino in the pathway. These findings were further extended and confirmed by examining the phenotypic consequences of extended poly(A) tract length variation. Although ORFs related to those of pglB2 are broadly distributed in eubacteria, they are primarily found as two distinct, juxtaposed ORFs. Thus, the neisserial pglB2 system provides novel insights into the potential influence of hypermutability on modular evolution of proteins by providing a unique snapshot of the progression of ongoing gene fusion. © 2013, American Society for Microbiology.

References Powered by Scopus

MEGA5: Molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods

36432Citations
N/AReaders
Get full text

The rapid generation of mutation data matrices from protein sequences

5920Citations
N/AReaders
Get full text

ProtTest 3: Fast selection of best-fit models of protein evolution

2130Citations
N/AReaders
Get full text

Cited by Powered by Scopus

The sweet tooth of bacteria: Common themes in bacterial glycoconjugates

113Citations
N/AReaders
Get full text

Neisseria meningitidis Type IV Pili Composed of Sequence Invariable Pilins Are Masked by Multisite Glycosylation

50Citations
N/AReaders
Get full text

Genetic determinants of genus—Level glycan diversity in a bacterial protein glycosylation system

16Citations
N/AReaders
Get full text

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Cite

CITATION STYLE

APA

Viburiene, R., Vik, A., Koomey, M., & Børud, B. (2013). Allelic variation in a simple sequence repeat element of neisserial pglB2 and its consequences for protein expression and protein glycosylation. Journal of Bacteriology, 195(15), 3476–3485. https://doi.org/10.1128/jb.00276-13

Readers' Seniority

Tooltip

PhD / Post grad / Masters / Doc 7

58%

Researcher 3

25%

Professor / Associate Prof. 1

8%

Lecturer / Post doc 1

8%

Readers' Discipline

Tooltip

Agricultural and Biological Sciences 7

54%

Biochemistry, Genetics and Molecular Bi... 4

31%

Medicine and Dentistry 1

8%

Chemistry 1

8%

Save time finding and organizing research with Mendeley

Sign up for free